Clare Woodward

5.2k total citations · 1 hit paper
84 papers, 4.4k citations indexed

About

Clare Woodward is a scholar working on Molecular Biology, Materials Chemistry and Spectroscopy. According to data from OpenAlex, Clare Woodward has authored 84 papers receiving a total of 4.4k indexed citations (citations by other indexed papers that have themselves been cited), including 75 papers in Molecular Biology, 32 papers in Materials Chemistry and 22 papers in Spectroscopy. Recurrent topics in Clare Woodward's work include Protein Structure and Dynamics (53 papers), Enzyme Structure and Function (31 papers) and Mass Spectrometry Techniques and Applications (17 papers). Clare Woodward is often cited by papers focused on Protein Structure and Dynamics (53 papers), Enzyme Structure and Function (31 papers) and Mass Spectrometry Techniques and Applications (17 papers). Clare Woodward collaborates with scholars based in United States, Japan and United Kingdom. Clare Woodward's co-authors include Jie Liang, Herbert Edelsbrunner, Bruce D. Hilton, J A Fuchs, George Bárány, Andreas Rosenberg, Erik Tüchsen, Renhao Li, Key Sun Kim and István Simon and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

Clare Woodward

84 papers receiving 4.1k citations

Hit Papers

Anatomy of protein pockets and cavities: Measurement of b... 1998 2026 2007 2016 1998 250 500 750

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Clare Woodward United States 37 3.6k 1.5k 988 896 376 84 4.4k
B. Lee United States 5 4.3k 1.2× 2.0k 1.4× 631 0.6× 466 0.5× 604 1.6× 6 5.5k
H.C. Watson United Kingdom 35 3.8k 1.0× 1.9k 1.3× 632 0.6× 1.2k 1.4× 418 1.1× 68 5.4k
William J. Cook United States 23 3.7k 1.0× 1.2k 0.8× 742 0.8× 445 0.5× 266 0.7× 43 4.7k
Kurt Wuethrich Switzerland 37 4.3k 1.2× 1.4k 0.9× 1.7k 1.7× 526 0.6× 403 1.1× 50 5.8k
Erik R. P. Zuiderweg United States 46 6.1k 1.7× 1.6k 1.1× 1.5k 1.5× 1.1k 1.2× 295 0.8× 137 7.6k
Kenneth P. Murphy United States 32 3.8k 1.0× 1.5k 1.0× 454 0.5× 334 0.4× 561 1.5× 52 5.2k
Ad Bax United States 25 3.8k 1.0× 1.4k 0.9× 1.4k 1.4× 296 0.3× 282 0.8× 30 4.7k
John F. Brandts United States 39 6.1k 1.7× 1.8k 1.2× 913 0.9× 684 0.8× 565 1.5× 71 8.0k
A.R. Fersht United Kingdom 32 3.6k 1.0× 1.9k 1.3× 435 0.4× 410 0.5× 270 0.7× 50 4.1k
Ruud M. Scheek Netherlands 33 3.3k 0.9× 1.1k 0.8× 1.1k 1.1× 259 0.3× 336 0.9× 87 4.0k

Countries citing papers authored by Clare Woodward

Since Specialization
Citations

This map shows the geographic impact of Clare Woodward's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Clare Woodward with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Clare Woodward more than expected).

Fields of papers citing papers by Clare Woodward

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Clare Woodward. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Clare Woodward. The network helps show where Clare Woodward may publish in the future.

Co-authorship network of co-authors of Clare Woodward

This figure shows the co-authorship network connecting the top 25 collaborators of Clare Woodward. A scholar is included among the top collaborators of Clare Woodward based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Clare Woodward. Clare Woodward is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Li, Renhao, John L. Battiste, & Clare Woodward. (2002). Native-like Interactions Favored in the Unfolded Bovine Pancreatic Trypsin Inhibitor Have Different Roles in Folding. Biochemistry. 41(7). 2246–2253. 8 indexed citations
2.
Sareth, Sina, Hua Li, Hiroaki Yamada, Clare Woodward, & Kazuyuki Akasaka. (2000). Rapid internal dynamics of BPTI is insensitive to pressure. FEBS Letters. 470(1). 11–14. 20 indexed citations
3.
Li, Renhao & Clare Woodward. (1999). The hydrogen exchange core and protein folding. Protein Science. 8(8). 1571–1590. 168 indexed citations
4.
Akasaka, Kazuyuki, et al.. (1999). Pressure response of protein backbone structure. Pressure‐induced amide 15N chemical shifts in BPTI. Protein Science. 8(10). 1946–1953. 79 indexed citations
5.
Barbar, Elisar, Michael Hare, Vladimir A. Daragan, George Bárány, & Clare Woodward. (1998). Dynamics of the Conformational Ensemble of Partially Folded Bovine Pancreatic Trypsin Inhibitor. Biochemistry. 37(21). 7822–7833. 19 indexed citations
6.
Ferrer, Marc, George Bárány, & Clare Woodward. (1995). Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor. Nature Structural & Molecular Biology. 2(3). 211–217. 49 indexed citations
7.
Barbar, Elisar, et al.. (1995). Extensive nonrandom structure in reduced and unfolded bovine pancreatic trypsin inhibitor. Biochemistry. 34(43). 13974–13981. 42 indexed citations
8.
Wilson, Nancy A., Elisar Barbar, J A Fuchs, & Clare Woodward. (1995). Aspartic Acid 26 in Reduced Escherichia coli Thioredoxin Has a pKa >9. Biochemistry. 34(28). 8931–8939. 42 indexed citations
9.
Danishefsky, Avis T., Dominique Housset, Alexander Wlodawer, et al.. (1993). Crevice‐forming mutants in the rigid core of bovine pancreatic trypsin inhibitor: Crystal structures of F22A, Y23A, N43G, and F45A. Protein Science. 2(4). 577–587. 24 indexed citations
10.
Kim, Key Sun & Clare Woodward. (1993). Protein internal flexibility and global stability: Effect of urea on hydrogen exchange rates of bovine pancreatic trypsin inhibitor. Biochemistry. 32(37). 9609–9613. 100 indexed citations
11.
Kim, Key Sun, J A Fuchs, & Clare Woodward. (1993). Hydrogen exchange identifies native-state motional domains important in protein folding. Biochemistry. 32(37). 9600–9608. 160 indexed citations
12.
Woodward, Clare. (1993). Is the slow-exchange core the protein folding core?. Trends in Biochemical Sciences. 18(10). 359–360. 83 indexed citations
13.
Gallagher, Warren H., Feng Tao, & Clare Woodward. (1992). Comparison of hydrogen exchange rates for bovine pancreatic trypsin inhibitor in crystals and in solution. Biochemistry. 31(19). 4673–4680. 28 indexed citations
14.
Ellis, Lynda B.M., et al.. (1992). Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon. Biochemistry. 31(20). 4882–4891. 27 indexed citations
17.
Woodward, Clare, et al.. (1982). Hydrogen exchange and the dynamic structure of proteins. Molecular and Cellular Biochemistry. 48(3). 135–160. 268 indexed citations
18.
Hilton, Bruce D. & Clare Woodward. (1979). Mechanism of isotope exchange kinetics of single protons in bovine pancreatic trypsin inhibitor. Biochemistry. 18(26). 5834–5841. 51 indexed citations
19.
Patel, Dinshaw J., Lita L. Canuel, Clare Woodward, & F. A. Bovey. (1975). Assignment of the histidine 12‐threonine 45 hydrogen‐bonded proton in the nmr spectrum of ribonuclease A in H2O. Biopolymers. 14(5). 959–974. 28 indexed citations
20.
Patel, Dinshaw J., Clare Woodward, & F. A. Bovey. (1972). Proton Nuclear Magnetic Resonance Studies of Ribonuclease A in H 2 O. Proceedings of the National Academy of Sciences. 69(3). 599–602. 24 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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